Post-translational modifications during lantibiotic biosynthesis

Research output: Contribution to journalReview article

Abstract

Recent reports have provided the first insights into the mechanisms of the extensive post-translational modifications involved in the biosynthesis of the lantibiotics, a class of peptide antimicrobial agents. These modifications involve dehydration of several serine and threonine residues followed by intramolecular conjugate additions of cysteines, resulting in extensively cross-linked polycyclic structures. Both in vivo and in vitro studies indicate low substrate specificity of the modification machinery, which has been explored for re-engineering of the structures of a number of members. In addition to these developments in understanding their biosynthesis, studies on the mode of action of several lantibiotics have shown a unique mechanism of binding to lipid II, an intermediate in cell wall biosynthesis.

Original languageEnglish (US)
Pages (from-to)498-507
Number of pages10
JournalCurrent Opinion in Chemical Biology
Volume8
Issue number5
DOIs
StatePublished - Oct 1 2004

Fingerprint

Bacteriocins
Biosynthesis
Post Translational Protein Processing
Threonine
Substrate Specificity
Anti-Infective Agents
Dehydration
Cell Wall
Serine
Cysteine
Peptides
Machinery
Cells
Substrates
In Vitro Techniques
muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol

Keywords

  • (Z)-2,3-dehydrobutyrine
  • 2,3-dehydroalanine
  • Dha
  • Dhb
  • Lan
  • MeLan
  • lanthionine
  • methyllanthionine

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

Cite this

Post-translational modifications during lantibiotic biosynthesis. / Xie, Lili; Van Der Donk, Wilfred A.

In: Current Opinion in Chemical Biology, Vol. 8, No. 5, 01.10.2004, p. 498-507.

Research output: Contribution to journalReview article

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